Lecture Four - Covalent Structures of Proteins

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  1. Define Primary Structure.
    Sequence of Amino Acid Residues
  2. Define Secondary Structure
    Local Spatial Conformation of Backbone
  3. Define Tertiary Structure
    Overall Fold or 3D arrangement of Polypeptide
  4. Define Quaternary Structure
    Spatial Arrangement of Subunits in a Multisubunit protein
  5. Secondary Structure is a result of Side chains. True of False?
    False, Secondary structure is independent of side chains
  6. What level of protein structure to Amino Acid side chains affect?
    Tertiary Structure (and upwards)
  7. What can a Protein's Primary Structure tell us?
    • Information about higher level structures
    • Evolutionary Relationships
    • Inherited Diseases
  8. Define Chemical Evolution.
    The Evolution of Amino Acid Sequences
  9. How do genes influence proteins?
    • Determining their Primary Structure
    • Specifying which Proteins are expressed
    • Specifying quantities of expressed protein
    • Specifying schedule of protein appearance
  10. If an otherwise successful organism gains a silent mutation, is it likely this mutation will propagate?
    Yes, propagation genarally occurs if the mutation has a positive effect or no effect at all
  11. In which proteins do mutations often lead to evolution?
    Developmental proteins that specify where and when something will be made
  12. What are some properties of a healthy red blood cell in low oxygen?
    • Irregular Crescent-like shape
    • Malleable/flexible
  13. Where might a red blood cell experience low oxygen ocnditions?
    In capillaries
  14. What are some properties of red blood cells in people with sickle cell anemia?
    • Rigid
    • Sickle-shaped
  15. How do the altered properties of red blood cells in people with sickle cell anemia cause problems?
    The rigid red blood cells can block blood vessels resulting in tissue damage
  16. What is Haemolytic anemia?
    Burtsting of red blood cells
  17. What is the two/three letter abbreviation of Haemoglobin;
    In a normal Person?
    In a person with Sickle Cell Anaemia?
    • Normal - Hb
    • Affected - HbS
  18. How is Haemoglobin different in people with Sickle Cell Anaemia?
    It has ~2 fewer negative charges
  19. What is Trypsin? What does it do?
    • An enzyme that digests protein
    • It cleaved after positive Amino Acids
  20. What is the Amino Acid residue mutation in HbS?
    Glu 6 is converted to Val 6
  21. What are the Haemoglobin Subunits called?
    • Alpha and Beta
    • There are two of each (four in total)
  22. How does Isoelectric focussing cause separation?
    By charge
  23. What disease does Sickle Cell anaemia give resistance to?
  24. What subunit is mutated in HbS?
    The Beta Subunit
  25. What organism causes Malaria?
    The protozoanĀ Plasmodium falciparum.
  26. How can you encourage HbS cells to sickle?
    Decrease the pH
  27. Define Homologous.
    Evolved or Derived from a Common Ancestor.
  28. Define Neutral Drift.
    Random Mutations in Well Adapted Proteins that do not affect function
  29. What is an Invariant Residue?
    A residue in the primary sequence with essential function, i.e it cannot mutate without loss of function.
  30. What are;
    Conservative Substitutions/Residues
    Non-Conservative Substitutions/Residues
    • Conservative - Can mutate to residues with similar functional properties.
    • Non-conservative - Hypervariable regions with a non-specific functional role.
  31. In what organisms do you find Cytochrome C?
    Oxygen using Eukaryotes
  32. What is Rate of Accumulation?
    The rate at which a protein in an organism develops changed as a result of mutations
  33. Why is the Rate of Accumulation less than the rate of Mutation?
    • Random Mutations are Reversible
    • Accumulation is limited by invariant and conservative residues
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Lecture Four - Covalent Structures of Proteins
2013-09-30 21:44:24
Biochemistry Lecture Four Covalent Stuctures Proteins

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